ID   GCSP_PSYCK              Reviewed;         965 AA.
AC   Q1QCL7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00711};
DE            EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine cleavage system P-protein {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine decarboxylase {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000255|HAMAP-Rule:MF_00711};
GN   Name=gcvP {ECO:0000255|HAMAP-Rule:MF_00711};
GN   OrderedLocusNames=Pcryo_0803;
OS   Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS   / K5).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=335284;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. The P protein binds the alpha-amino group of glycine through
CC       its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC       methylamine moiety is then transferred to the lipoamide cofactor of the
CC       H protein. {ECO:0000255|HAMAP-Rule:MF_00711}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; Xref=Rhea:RHEA:24304,
CC         Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83143; EC=1.4.4.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00711};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00711};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000255|HAMAP-Rule:MF_00711}.
CC   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000255|HAMAP-
CC       Rule:MF_00711}.
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DR   EMBL; CP000323; ABE74586.1; -; Genomic_DNA.
DR   RefSeq; WP_011513150.1; NC_007969.1.
DR   AlphaFoldDB; Q1QCL7; -.
DR   SMR; Q1QCL7; -.
DR   STRING; 335284.Pcryo_0803; -.
DR   KEGG; pcr:Pcryo_0803; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_1_6; -.
DR   Proteomes; UP000002425; Chromosome.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR049315; GDC-P_N.
DR   InterPro; IPR020581; GDC_P.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate.
FT   CHAIN           1..965
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045596"
FT   MOD_RES         711
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   965 AA;  105692 MW;  02AA48F292B797E9 CRC64;
     MTISQNPALD TFEGLFNEAE FVYRHLGSND AKQADLLSAI GYSDMATFIN ETVPEPVRLH
     KELDLPVAMS EHAALAKLRT MADDITVNKS YIGQGYSPVR MPAVIQRNVL ENPGWYTAYT
     PYQAEIAQGR LEALLNFQQV CIDLTGLELA GASLLDEATA AAEAMAMSKR VSKSKSMQFF
     VDDRVYPQTL DVINTRAKYF GWEVVVGDFE LAKSGDYFGA LFQYVGVEGD VKDLTDVIAA
     VKKNKTYVSV VSDIMSLVLL KSPADMGADV ALGSTQRFGI PMGFGGPHAA YFAFSDKAKR
     SAPGRIIGVS KDSQGNTALR MALQTREQHI RREKANSNIC TSQVLLANLA GMYAVYHGPG
     GVKRIATRIH AFATAFADVI KNANDSNLNV LHDQFFDSVV VDCGSEKLAS QIFQNADNVG
     YNLWRLGETK LSVAFSETSD QKDFNVLTQL FVTKAHDLPE DARVSLDSAH LRTDAILSHP
     VFNSHHTEHE MLRYLKSLED KDLAMNRSMI SLGSCTMKLN ATSEMLPITW PEFANVHPFA
     PRDQVTGYVA MIDSLQEQLK AITGFDDVSM QPNSGASGEY AGLLAIRRYH ESLGETDRDV
     CLIPMSAHGT NPATAMMMGM KVVVVKTDDN GNVDIDDLTA KSEEHSTRLG ALMITYPSTH
     GVFEEGIRKI CDLIHKHGGQ VYMDGANMNA QVGMMQPADV GADVLHMNLH KTFCIPHGGG
     GPGMGPIGMK AHLAPFMANH TLSPVHNAQK DCSAVSAAPY GSASILPISW MYIAMMGRDG
     LLKATELALL NANYVAAELK DHYPVLYTGK NGRVAHECII DIRPLKEETG ISESDIAKRL
     MDYGFHSPTM SFPVAGTLMI EPTESESKEE LDRFISALKS IKAEALKAKA GEDNWTLENN
     PLVNAPHTAA MVIDGEWTYP YSRETAAFPL PYIRTNKFWP SVARVDDAYG DKNLMCSCPS
     IENYM
//